The study reported that its effects were similar to those seen when proteinase K was applied in the same manner.

Subsequently, proteinase K was added and incubated again overnight.

Sections were permeabilised in a solution of proteinase K and the reaction stopped by immersion in 4% paraformaldehyde.

SecB has a proteolytic-sensitive domain that is cleaved by proteinase K in a limited proteolysis reaction.

DNA was extracted from tail clips by proteinase K digestion followed by ethanol precipitation.

This gene encodes a proprotein convertase belonging to the proteinase K subfamily of the secretory subtilase family.

The sections were digested with proteinase K, acetylated, washed and dehydrated as previously described [ 10 26 ] .

Removal of calcium from proteinase K gives rise to small but long-range structural changes affecting the active site, which is 17Å away from the metal site.

Viral DNA was purified from intracellular core particles by proteinase K digestion, phenol and chloroform extraction, and ethanol precipitation.

That binding receptor, a protein was proved by preincubating the OMPs with proteinase K that abolished all the binding activity of the iron siderophore complex (Fig.

Pepsin and proteinase K were tested with all four non-protease unmasking steps and protease VIII was only tested in combination with sodium citrate unmasking.

The pooled endoscopic biopsy specimens were thawed, homogenised, and incubated in sodium dodecyl sulphate and proteinase K (Boehringer, East Sussex, UK).

To purify the DNA, proteinase K is added to digest the antibodies and release the DNA, which can be collected and prepared for DNA detection.

Paraffin-embedded sections (10 μm in thickness) were microdissected following deparaffinization, and the tissue was then digested by proteinase K in tris-EDTA buffer at 55 C for 4 hr.

(2) Sections were pretreated with proteinase K before heating; intensive staining of non-apoptotic nuclei demonstrates that the procedure detects decreased DNA stability induced by the digestion of nuclear proteins.

To determine the nature of the binding receptor, the OMP preparation was subjected to digestion with proteinase K (10 mg/ml) for 1 hr at 37 C prior to the incubation with iron siderophore complex.

Post-digestion fixation Including post-digestion fixation steps with 4% paraformaldehyde or methanol/acetic acid (4:1) in the NISH assay were investigated when pepsin or proteinase K were used with or without sodium citrate.

PrP is readily digested by proteinase K and can be liberated from the cell surface in vitro by the enzyme phosphoinositide phospholipase C (PI-PLC), which cleaves the glycophosphatidylinositol (GPI) glycolipid anchor.

The parafin embedded specimens were first digested with proteinase K and subsequently coated with 1/100 dilution of anti-delta antibody positive human serum and then with a rabbit anti-human IgG (1/16 diluted, Dako, Accurate Chem).

Studies that used proteinase K to cleave VPg from the viral genome discovered that calicivirus vesicular exanthema virus lacking VPg is no longer infectious whereas poliovirus retains infectivity even with the absence of VPg.

Scott Bronson, the lab instructor, explained that the enzyme, proteinase K, digests the membrane that holds in place the cells containing the DNA; when the temperature is raised to boiling, the cells break open, letting the DNA out.

For example, proteinase K, a broad spectrum proteinase stable in urea and SDS, is often used in the preparation of nucleic acids to remove unwanted nuclease contaminants which may otherwise degrade the DNA or RNA.

In contrast to previously described methods for detection of PrP in brain homogenates, these techniques, when used to study brain homogenates, do not use seeded polymerization, amplification, or enzymatic digestion (for example, by proteinase K, or "PK").

The mixture was digested with 400 μg/ml proteinase K in the presence of 1% SDS for 2 h at 37 C. After phenol and chloroform extraction, the DNA was precipitated with ethanol, resolved on a 1.2% agarose gel and detected by autoradiography.

Residual proteins are often removed by enzymatic digestion using sodium dodecyl sulfate (SDS) /proteinase K, but the physical separation of the proteins from the nucleic acids is accomplished by centrifugation of a mixture of the nucleic acid solution and phenol and chloroform.